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Database: UniProt
Entry: E0PZ12_9STRE
LinkDB: E0PZ12_9STRE
Original site: E0PZ12_9STRE 
ID   E0PZ12_9STRE            Unreviewed;        92 AA.
AC   E0PZ12;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN   Name=acyP {ECO:0000313|EMBL:EFM36231.1};
GN   ORFNames=HMPREF9189_0043 {ECO:0000313|EMBL:EFM36231.1};
OS   Streptococcus sp. oral taxon 071 str. 73H25AP.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=864570 {ECO:0000313|EMBL:EFM36231.1, ECO:0000313|Proteomes:UP000005184};
RN   [1] {ECO:0000313|EMBL:EFM36231.1, ECO:0000313|Proteomes:UP000005184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73H25AP {ECO:0000313|EMBL:EFM36231.1,
RC   ECO:0000313|Proteomes:UP000005184};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC         ProRule:PRU00520};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFM36231.1}.
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DR   EMBL; AEEP01000004; EFM36231.1; -; Genomic_DNA.
DR   RefSeq; WP_001174622.1; NZ_GL397254.1.
DR   AlphaFoldDB; E0PZ12; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_2_1_9; -.
DR   Proteomes; UP000005184; Unassembled WGS sequence.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW   ECO:0000313|EMBL:EFM36231.1}.
FT   DOMAIN          3..92
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   92 AA;  10234 MW;  233927C1E4517157 CRC64;
     MQKVRMIVQG RVQGVGFRWG VYTLALEIGG ITGRVWNNDD GTVEILAQAD SSATMAKFIQ
     EIRKGPTPFS KVTYLDVQMS NFSSYPDFKV AN
//
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